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S. aureus peptidoglycan hydrolysis by mutanolysin and LytM catalytic domain

ABSTRACT: (Manuscript abstract) "Peptidoglycan, a gigadalton polymer, functions as the scaffold for bacterial cell walls and provides cell integrity. Peptidoglycan is remodelled by a large and diverse group of peptidoglycan hydrolases, which control bacterial cell growth and division. Over the years, many studies have focused on these enzymes, but knowledge on their action within peptidoglycan mesh from a molecular basis is scarce. Here, we provide structural insights into the interaction between short peptidoglycan fragments and the entire sacculus with two evolutionarily related peptidases of the M23 family, lysostaphin and LytM. Through nuclear magnetic resonance, mass spectrometry, information-driven modelling, site-directed mutagenesis and biochemical approaches, we propose a model in which peptidoglycan cross-linking affects the activity, selectivity and specificity of these two structurally related enzymes differently."

INSTRUMENT(S): Synapt MS

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Alicja Razew

LAB HEAD: Izabela Sabala

PROVIDER: PXD045859 | Pride | 2023-11-06

REPOSITORIES: Pride

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	220331AliW_Mut_LytM.mzXML	Mzxml
	220331AliW_Mut_LytM.raw.zip	Raw
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